Primary sequence determinants responsible for site‐selective dephosphorylation of the PDGF β‐receptor by the receptor‐like protein tyrosine phosphatase DEP‐1

FEBS Letters

Engström, Ulla²  Östman, Arne²  Persson, Camilla²  Mowbray, Sherry L¹ 

[1] Department of Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Center, P.O. Box 590, SE-751 24 Uppsala, Sweden;Ludwig Institute for Cancer Research, Biomedical Center, P.O. Box 595, SE-751 24 Uppsala, Sweden

关键词: Protein tyrosine phosphatase;    Substrate specificity;    Phospho-peptide;    DEP-1;    PDGF β-receptor;   

DOI  :  10.1016/S0014-5793(02)02570-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Site-selective dephosphorylation of receptor tyrosine kinases contributes to receptor regulation. The receptor-like protein tyrosine phosphatase DEP-1 site-selectively dephosphorylates the PDGF β-receptor. DEP-1 dephosphorylation of original and chimeric phospho-peptides spanning the preferred pY1021 and the less preferred pY857 and pY562 sites was analyzed. Double substitutions of basic residues at −4 and +3 of pY857 and pY562 peptides improved affinity. Substitutions of single amino acids indicated preference for an acidic residue at position −1 and a preference against a basic residue at position +3. DEP-1 site-selective dephosphorylation of PDGF β-receptor is thus determined by the primary sequence surrounding phosphorylation sites and involves interactions with residues spanning at least between positions −1 and +3.

【 授权许可】

Unknown